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Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases

✍ Scribed by Istvan Botos; Edward E. Melnikov; Scott Cherry; Serguei Kozlov; Oksana V. Makhovskaya; Joseph E. Tropea; Alla Gustchina; Tatyana V. Rotanova; Alexander Wlodawer

Book ID: 116662260
Publisher: Elsevier Science
Year: 2005
Tongue: English
Weight: 713 KB
Volume: 351
Category: Article
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2005.06.008

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## Abstract The key residue of the active site of triosephosphate isomerase (TIM) is the catalytic glutamate, which is proposed to be important (i) as a catalytic base, for initiating the reaction, as well as (ii) for the subsequent proton shuttling steps. The structural properties of this glutamat